Low resolution solution structure of the Apo form of Escherichia coli haemoglobin protease Hbp.
Low resolution solution structure of the Apo form of Escherichia coli haemoglobin protease Hbp.
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大肠杆菌血红蛋白蛋白酶 Hbp Apo 形式的低分辨率溶液结构。
DOI：
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发表时间：
2002
影响因子：
5.6
通讯作者：
B. Otto
中科院分区：
文献类型：
--
作者：
D. Scott;J. Grossmann;J. Tame;O. Byron;K. Wilson;B. Otto
我们已经研究了血红蛋白蛋白酶或“血红蛋白酶”，Hbp，一个重要的铁收购系统在致病性大肠杆菌的主要组成部分的apo形式的解决方案的性质。实验测定的二级结构含量从圆二色性（CD）光谱，获得使用同步辐射光，表明该蛋白质主要包含β-片层与二级结构预测从一级序列。接下来，使用分析超离心（AUC）和小角X射线散射（SAXS）探测蛋白质的大小和形状。这表明Hbp是一个单体，具有延伸的构象。使用从头计算重建方法，我们已经产生了一个模型的Hbp，这表明该蛋白质采用扩展的新月形构象。所得模型的分析得到的流体动力学参数与实验观察到的一致。因此，我们能够构建溶液中apo-Hbp的流体动力学严格模型，不仅为SAXS重建方法的结果提供了更大的置信度，而且提供了这个有趣分子的第一个三维视图。
We have studied the solution properties of the apo form of the haemoglobin protease or "haemoglobinase", Hbp, a principal component of an important iron acquisition system in pathogenic Escherichia coli. Experimental determination of secondary structure content from circular dichroism (CD) spectroscopy, obtained using synchrotron light, showed that the protein contains predominately beta-sheets in agreement with secondary structure prediction from the primary sequence. Next, the size and shape of the protein were probed using analytical ultracentrifugation (AUC) and small angle X-ray scattering (SAXS). These showed that Hbp is a monomer, with an extended conformation. Using ab initio reconstruction methods we have produced a model of Hbp, which shows that the protein adopts an extended crescent-shaped conformation. Analysis of the resulting model gives hydrodynamic parameters in good agreement with those observed experimentally. Thus we are able to construct a hydrodynamically rigorous model of apo-Hbp in solution, not only giving a greater level of confidence to the results of the SAXS reconstruction methods, but providing the first three-dimensional view of this intriguing molecule.
影响因子：
3.4
作者：
JOHNSON, ML;CORREIA, JJ;HALVORSON, HR
通讯作者：
HALVORSON, HR
影响因子：
4.3
作者：
WHITE, JV;STULTZ, CM;SMITH, TF
通讯作者：
SMITH, TF